Platelet-derived growth factor induces multisite phosphorylation of pp60c-src and increases its protein-tyrosine kinase activity.

摘要: Abstract We have shown previously that pp60c-src is a substrate for protein kinase C in vivo and the target of phosphorylation mammalian serine 12. We now demonstrate addition to tumor promoters, all activators phosphatidylinositol turnover we tested fibroblasts (platelet-derived growth factor, fibroblast serum, vasopressin, sodium orthovanadate, prostaglandin F2 alpha) lead at In stimulating 12 pp60c-src, platelet-derived factor treatment quiescent induces one or two additional residues tyrosine residue within N-terminal 16 kilodaltons enzyme activates its immune complex protein-tyrosine activity.